Disease resistance of Arabidopsis to Phytophthora brassicae is established by the sequential action of indole glucosinolates and camalexin.
Identifieur interne : 001949 ( Main/Exploration ); précédent : 001948; suivant : 001950Disease resistance of Arabidopsis to Phytophthora brassicae is established by the sequential action of indole glucosinolates and camalexin.
Auteurs : Klaus Schlaeppi [Suisse] ; Eliane Abou-Mansour ; Antony Buchala ; Felix MauchSource :
- The Plant journal : for cell and molecular biology [ 1365-313X ] ; 2010.
Descripteurs français
- KwdFr :
- ARN des plantes (génétique), Arabidopsis (génétique), Arabidopsis (immunologie), Arabidopsis (métabolisme), Glucosinolates (métabolisme), Immunité innée (MeSH), Indoles (métabolisme), Maladies des plantes (génétique), Maladies des plantes (immunologie), Mutation (MeSH), Phytophthora (physiologie), Régulation de l'expression des gènes végétaux (MeSH), Thiazoles (métabolisme).
- MESH :
- génétique : ARN des plantes, Arabidopsis, Maladies des plantes.
- immunologie : Arabidopsis, Maladies des plantes.
- métabolisme : Arabidopsis, Glucosinolates, Indoles, Thiazoles.
- physiologie : Phytophthora.
- Immunité innée, Mutation, Régulation de l'expression des gènes végétaux.
English descriptors
- KwdEn :
- Arabidopsis (genetics), Arabidopsis (immunology), Arabidopsis (metabolism), Gene Expression Regulation, Plant (MeSH), Glucosinolates (metabolism), Immunity, Innate (MeSH), Indoles (metabolism), Mutation (MeSH), Phytophthora (physiology), Plant Diseases (genetics), Plant Diseases (immunology), RNA, Plant (genetics), Thiazoles (metabolism).
- MESH :
- chemical , genetics : RNA, Plant.
- chemical , metabolism : Glucosinolates, Indoles, Thiazoles.
- genetics : Arabidopsis, Plant Diseases.
- immunology : Arabidopsis, Plant Diseases.
- metabolism : Arabidopsis.
- physiology : Phytophthora.
- Gene Expression Regulation, Plant, Immunity, Innate, Mutation.
Abstract
We have analysed the role of tryptophan-derived secondary metabolites in disease resistance of Arabidopsis to the oomycete pathogen Phytophthora brassicae. Transcript analysis revealed that genes encoding enzymes involved in tryptophan, camalexin and indole glucosinolate (iGS) biosynthesis are coordinately induced in response to P. brassicae. However, a deficiency in either camalexin or iGS accumulation has only a minor effect on the disease resistance of Arabidopsis mutants. In contrast, the double mutant cyp79B2 cyp79B3, which has a blockage in the production of indole-3-aldoxime (IAOx), the common precursor of tryptophan-derived metabolites including camalexin and iGS, is highly susceptible to P. brassicae. Because cyp79B2 cyp79B3 shows no deficiencies in other tested disease resistance responses, we concluded that the lack of IAOx-derived compounds renders Arabidopsis susceptible despite wild-type-like pathogen-induced hypersensitive cell death, stress hormone signaling and callose deposition. The susceptibility of the double mutant pen2-1 pad3-1, which has a combined defect in camalexin synthesis and PEN2-catalysed hydrolysis of iGS compounds, demonstrates that both camalexin and products of iGS hydrolysis are important for disease resistance to P. brassicae. Products of iGS hydrolysis play an early defensive role, as indicated by enhanced epidermal penetration rates of Arabidopsis mutants affected in iGS synthesis or degradation. Our results show that disease resistance of Arabidopsis to P. brassicae is established by the sequential activity of the phytoanticipin iGS and the phytoalexin camalexin.
DOI: 10.1111/j.1365-313X.2010.04197.x
PubMed: 20230487
Affiliations:
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innée</term><term>Mutation</term><term>Régulation de l'expression des gènes végétaux</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have analysed the role of tryptophan-derived secondary metabolites in disease resistance of Arabidopsis to the oomycete pathogen Phytophthora brassicae. Transcript analysis revealed that genes encoding enzymes involved in tryptophan, camalexin and indole glucosinolate (iGS) biosynthesis are coordinately induced in response to P. brassicae. However, a deficiency in either camalexin or iGS accumulation has only a minor effect on the disease resistance of Arabidopsis mutants. In contrast, the double mutant cyp79B2 cyp79B3, which has a blockage in the production of indole-3-aldoxime (IAOx), the common precursor of tryptophan-derived metabolites including camalexin and iGS, is highly susceptible to P. brassicae. Because cyp79B2 cyp79B3 shows no deficiencies in other tested disease resistance responses, we concluded that the lack of IAOx-derived compounds renders Arabidopsis susceptible despite wild-type-like pathogen-induced hypersensitive cell death, stress hormone signaling and callose deposition. The susceptibility of the double mutant pen2-1 pad3-1, which has a combined defect in camalexin synthesis and PEN2-catalysed hydrolysis of iGS compounds, demonstrates that both camalexin and products of iGS hydrolysis are important for disease resistance to P. brassicae. Products of iGS hydrolysis play an early defensive role, as indicated by enhanced epidermal penetration rates of Arabidopsis mutants affected in iGS synthesis or degradation. Our results show that disease resistance of Arabidopsis to P. brassicae is established by the sequential activity of the phytoanticipin iGS and the phytoalexin camalexin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20230487</PMID><DateCompleted><Year>2010</Year><Month>09</Month><Day>16</Day></DateCompleted><DateRevised><Year>2010</Year><Month>06</Month><Day>11</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-313X</ISSN><JournalIssue CitedMedium="Internet"><Volume>62</Volume><Issue>5</Issue><PubDate><Year>2010</Year><Month>Jun</Month><Day>01</Day></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>Disease resistance of Arabidopsis to Phytophthora brassicae is established by the sequential action of indole glucosinolates and camalexin.</ArticleTitle><Pagination><MedlinePgn>840-51</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1365-313X.2010.04197.x</ELocationID><Abstract><AbstractText>We have analysed the role of tryptophan-derived secondary metabolites in disease resistance of Arabidopsis to the oomycete pathogen Phytophthora brassicae. Transcript analysis revealed that genes encoding enzymes involved in tryptophan, camalexin and indole glucosinolate (iGS) biosynthesis are coordinately induced in response to P. brassicae. However, a deficiency in either camalexin or iGS accumulation has only a minor effect on the disease resistance of Arabidopsis mutants. In contrast, the double mutant cyp79B2 cyp79B3, which has a blockage in the production of indole-3-aldoxime (IAOx), the common precursor of tryptophan-derived metabolites including camalexin and iGS, is highly susceptible to P. brassicae. Because cyp79B2 cyp79B3 shows no deficiencies in other tested disease resistance responses, we concluded that the lack of IAOx-derived compounds renders Arabidopsis susceptible despite wild-type-like pathogen-induced hypersensitive cell death, stress hormone signaling and callose deposition. The susceptibility of the double mutant pen2-1 pad3-1, which has a combined defect in camalexin synthesis and PEN2-catalysed hydrolysis of iGS compounds, demonstrates that both camalexin and products of iGS hydrolysis are important for disease resistance to P. brassicae. Products of iGS hydrolysis play an early defensive role, as indicated by enhanced epidermal penetration rates of Arabidopsis mutants affected in iGS synthesis or degradation. Our results show that disease resistance of Arabidopsis to P. brassicae is established by the sequential activity of the phytoanticipin iGS and the phytoalexin camalexin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schlaeppi</LastName><ForeName>Klaus</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, Fribourg, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Abou-Mansour</LastName><ForeName>Eliane</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Buchala</LastName><ForeName>Antony</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Mauch</LastName><ForeName>Felix</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018749" MajorTopicYN="N">RNA, Plant</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013844" MajorTopicYN="N">Thiazoles</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>3</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>3</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>9</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20230487</ArticleId><ArticleId IdType="pii">TPJ4197</ArticleId><ArticleId IdType="doi">10.1111/j.1365-313X.2010.04197.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country><region><li>Canton de Fribourg</li></region><settlement><li>Fribourg</li></settlement><orgName><li>Université de Fribourg</li></orgName></list><tree><noCountry><name sortKey="Abou Mansour, Eliane" sort="Abou Mansour, Eliane" uniqKey="Abou Mansour E" first="Eliane" last="Abou-Mansour">Eliane Abou-Mansour</name><name sortKey="Buchala, Antony" sort="Buchala, Antony" uniqKey="Buchala A" first="Antony" last="Buchala">Antony Buchala</name><name sortKey="Mauch, Felix" sort="Mauch, Felix" uniqKey="Mauch F" first="Felix" last="Mauch">Felix Mauch</name></noCountry><country name="Suisse"><region name="Canton de Fribourg"><name sortKey="Schlaeppi, Klaus" sort="Schlaeppi, Klaus" uniqKey="Schlaeppi K" first="Klaus" last="Schlaeppi">Klaus Schlaeppi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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